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3JAR

Cryo-EM structure of GDP-microtubule co-polymerized with EB3

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000226biological_processmicrotubule cytoskeleton organization
A0000278biological_processmitotic cell cycle
A0003924molecular_functionGTPase activity
A0005200molecular_functionstructural constituent of cytoskeleton
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0007017biological_processmicrotubule-based process
A0015630cellular_componentmicrotubule cytoskeleton
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000226biological_processmicrotubule cytoskeleton organization
B0000278biological_processmitotic cell cycle
B0001764biological_processneuron migration
B0003924molecular_functionGTPase activity
B0005200molecular_functionstructural constituent of cytoskeleton
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0007017biological_processmicrotubule-based process
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0000226biological_processmicrotubule cytoskeleton organization
C0000278biological_processmitotic cell cycle
C0003924molecular_functionGTPase activity
C0005200molecular_functionstructural constituent of cytoskeleton
C0005525molecular_functionGTP binding
C0005737cellular_componentcytoplasm
C0005856cellular_componentcytoskeleton
C0005874cellular_componentmicrotubule
C0007017biological_processmicrotubule-based process
C0015630cellular_componentmicrotubule cytoskeleton
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0000226biological_processmicrotubule cytoskeleton organization
D0000278biological_processmitotic cell cycle
D0001764biological_processneuron migration
D0003924molecular_functionGTPase activity
D0005200molecular_functionstructural constituent of cytoskeleton
D0005515molecular_functionprotein binding
D0005525molecular_functionGTP binding
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0005874cellular_componentmicrotubule
D0007017biological_processmicrotubule-based process
D0046872molecular_functionmetal ion binding
E0000166molecular_functionnucleotide binding
E0000226biological_processmicrotubule cytoskeleton organization
E0000278biological_processmitotic cell cycle
E0003924molecular_functionGTPase activity
E0005200molecular_functionstructural constituent of cytoskeleton
E0005525molecular_functionGTP binding
E0005737cellular_componentcytoplasm
E0005856cellular_componentcytoskeleton
E0005874cellular_componentmicrotubule
E0007017biological_processmicrotubule-based process
E0015630cellular_componentmicrotubule cytoskeleton
E0016787molecular_functionhydrolase activity
E0046872molecular_functionmetal ion binding
F0000166molecular_functionnucleotide binding
F0000226biological_processmicrotubule cytoskeleton organization
F0000278biological_processmitotic cell cycle
F0001764biological_processneuron migration
F0003924molecular_functionGTPase activity
F0005200molecular_functionstructural constituent of cytoskeleton
F0005515molecular_functionprotein binding
F0005525molecular_functionGTP binding
F0005737cellular_componentcytoplasm
F0005856cellular_componentcytoskeleton
F0005874cellular_componentmicrotubule
F0007017biological_processmicrotubule-based process
F0046872molecular_functionmetal ion binding
G0000166molecular_functionnucleotide binding
G0000226biological_processmicrotubule cytoskeleton organization
G0000278biological_processmitotic cell cycle
G0001764biological_processneuron migration
G0003924molecular_functionGTPase activity
G0005200molecular_functionstructural constituent of cytoskeleton
G0005515molecular_functionprotein binding
G0005525molecular_functionGTP binding
G0005737cellular_componentcytoplasm
G0005856cellular_componentcytoskeleton
G0005874cellular_componentmicrotubule
G0007017biological_processmicrotubule-based process
G0046872molecular_functionmetal ion binding
H0000166molecular_functionnucleotide binding
H0000226biological_processmicrotubule cytoskeleton organization
H0000278biological_processmitotic cell cycle
H0001764biological_processneuron migration
H0003924molecular_functionGTPase activity
H0005200molecular_functionstructural constituent of cytoskeleton
H0005515molecular_functionprotein binding
H0005525molecular_functionGTP binding
H0005737cellular_componentcytoplasm
H0005856cellular_componentcytoskeleton
H0005874cellular_componentmicrotubule
H0007017biological_processmicrotubule-based process
H0046872molecular_functionmetal ion binding
I0000166molecular_functionnucleotide binding
I0000226biological_processmicrotubule cytoskeleton organization
I0000278biological_processmitotic cell cycle
I0001764biological_processneuron migration
I0003924molecular_functionGTPase activity
I0005200molecular_functionstructural constituent of cytoskeleton
I0005515molecular_functionprotein binding
I0005525molecular_functionGTP binding
I0005737cellular_componentcytoplasm
I0005856cellular_componentcytoskeleton
I0005874cellular_componentmicrotubule
I0007017biological_processmicrotubule-based process
I0046872molecular_functionmetal ion binding
J0000166molecular_functionnucleotide binding
J0000226biological_processmicrotubule cytoskeleton organization
J0000278biological_processmitotic cell cycle
J0003924molecular_functionGTPase activity
J0005200molecular_functionstructural constituent of cytoskeleton
J0005525molecular_functionGTP binding
J0005737cellular_componentcytoplasm
J0005856cellular_componentcytoskeleton
J0005874cellular_componentmicrotubule
J0007017biological_processmicrotubule-based process
J0015630cellular_componentmicrotubule cytoskeleton
J0016787molecular_functionhydrolase activity
J0046872molecular_functionmetal ion binding
K0000166molecular_functionnucleotide binding
K0000226biological_processmicrotubule cytoskeleton organization
K0000278biological_processmitotic cell cycle
K0003924molecular_functionGTPase activity
K0005200molecular_functionstructural constituent of cytoskeleton
K0005525molecular_functionGTP binding
K0005737cellular_componentcytoplasm
K0005856cellular_componentcytoskeleton
K0005874cellular_componentmicrotubule
K0007017biological_processmicrotubule-based process
K0015630cellular_componentmicrotubule cytoskeleton
K0016787molecular_functionhydrolase activity
K0046872molecular_functionmetal ion binding
L0000166molecular_functionnucleotide binding
L0000226biological_processmicrotubule cytoskeleton organization
L0000278biological_processmitotic cell cycle
L0003924molecular_functionGTPase activity
L0005200molecular_functionstructural constituent of cytoskeleton
L0005525molecular_functionGTP binding
L0005737cellular_componentcytoplasm
L0005856cellular_componentcytoskeleton
L0005874cellular_componentmicrotubule
L0007017biological_processmicrotubule-based process
L0015630cellular_componentmicrotubule cytoskeleton
L0016787molecular_functionhydrolase activity
L0046872molecular_functionmetal ion binding
M0008017molecular_functionmicrotubule binding
N0008017molecular_functionmicrotubule binding
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE GTP E 501
ChainResidue
EGLY10
EGLY143
EGLY144
ETHR145
EGLY146
EILE171
ETHR179
EGLU183
EASN206
ETYR224
EASN228
EGLN11
EMG502
GLEU248
GLYS254
EALA12
EGLN15
EASP98
EALA99
EALA100
EASN101
ESER140

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG E 502
ChainResidue
EGLU71
EGTP501

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GDP F 501
ChainResidue
FGLN11
FCYS12
FGLN15
FSER140
FGLY143
FGLY144
FTHR145
FGLY146
FASP179
FASN206
FTYR224
FASN228

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GTP J 501
ChainResidue
FLEU248
FLYS254
JGLN11
JALA12
JGLN15
JALA99
JASN101
JSER140
JGLY143
JGLY144
JTHR145
JGLY146
JILE171
JTHR179
JGLU183
JASN206
JTYR224
JASN228
JMG502

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG J 502
ChainResidue
JGLU71
JGTP501

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GDP G 501
ChainResidue
GGLN11
GCYS12
GGLN15
GSER140
GGLY143
GGLY144
GTHR145
GGLY146
GASP179
GASN206
GTYR224
GASN228

site_idAC7
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GTP C 501
ChainResidue
CGLN11
CALA12
CGLN15
CALA99
CALA100
CASN101
CSER140
CGLY143
CGLY144
CTHR145
CGLY146
CILE171
CTHR179
CGLU183
CASN206
CTYR224
CASN228
CMG502
ILEU248
ILYS254

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG C 502
ChainResidue
CGLU71
CGTP501

site_idAC9
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GDP D 501
ChainResidue
DASP179
DASN206
DTYR224
DASN228
DGLN11
DCYS12
DGLN15
DSER140
DGLY143
DGLY144
DTHR145
DGLY146

site_idBC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GTP L 501
ChainResidue
DLEU248
DLYS254
LGLN11
LALA12
LGLN15
LALA99
LASN101
LSER140
LGLY143
LGLY144
LTHR145
LGLY146
LILE171
LTHR179
LGLU183
LASN206
LTYR224
LASN228
LMG502

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG L 502
ChainResidue
LGLU71
LGTP501

site_idBC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GDP I 501
ChainResidue
IGLN11
ICYS12
IGLN15
ISER140
IGLY143
IGLY144
ITHR145
IGLY146
IASP179
IASN206
ITYR224
IASN228

site_idBC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GTP A 501
ChainResidue
AGLN11
AALA12
AGLN15
AASP98
AALA99
AALA100
AASN101
ASER140
AGLY143
AGLY144
ATHR145
AGLY146
AILE171
ATHR179
AGLU183
AASN206
ATYR224
AASN228
AMG502
HLEU248
HLYS254

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
AGLU71
AGTP501

site_idBC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GDP B 501
ChainResidue
BGLN11
BCYS12
BGLN15
BSER140
BGLY143
BGLY144
BTHR145
BGLY146
BASP179
BASN206
BTYR224
BASN228

site_idBC7
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GTP K 501
ChainResidue
BLEU248
BLYS254
KGLN11
KALA12
KGLN15
KASP98
KALA99
KALA100
KASN101
KSER140
KGLY143
KGLY144
KTHR145
KGLY146
KILE171
KTHR179
KGLU183
KASN206
KTYR224
KASN228
KMG502

site_idBC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG K 502
ChainResidue
KGLU71
KGTP501

site_idBC9
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GDP H 501
ChainResidue
HGLN11
HCYS12
HGLN15
HSER140
HGLY143
HGLY144
HTHR145
HGLY146
HASP179
HASN206
HTYR224
HASN228

Functional Information from PROSITE/UniProt
site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
ChainResidueDetails
EGLY142-GLY148
FGLY142-GLY148

site_idPS00228
Number of Residues4
DetailsTUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI
ChainResidueDetails
FMET1-ILE4

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsMotif: {"description":"MREC motif","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues108
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues18
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues18
DetailsMotif: {"description":"MREI motif","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues42
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues6
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"UniProtKB","id":"Q13885","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues12
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues6
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues12
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues204
DetailsDomain: {"description":"Calponin-homology (CH)","evidences":[{"source":"PROSITE-ProRule","id":"PRU00044","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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